Binding affinity of bicarboxylate ions for cobalt(II) bovine carbonic anhydrase

✍ Scribed by I. Bertini; C. Luchinat; A. Scozzafava

• Book ID: 104106022
• Publisher: Elsevier Science
• Year: 1978
• Weight: 414 KB
• Volume: 9
• Category: Article
• ISSN: 0006-3061
• DOI: 10.1016/s0006-3061(00)80283-5

✦ Synopsis

The affinity of bicarboxylate ions (from oxaiate to glutarate) for cobalt(E) bovine carbonic anhydrase has been investigated and compared with that cf acetate and propionate. The oxalate ion shows a much greater affiiity for the enzyme than acetate. whereas the other bicarboxylate ions have very little tendency to bind the enzyme. In every case, and particulariy for the oxalate, the apparent affkity constants dramatically increase with decreasing pH. On the basis of the electronic spectra a five-coordinate structure is proposed for all of the above derivatives.

Carbon-13 NMR data have been discussed in terms of the oxalate ion chelating the metal ion and/or interacting with the wall of the active cavity.